| The normal, cellular prion protein, designated PrPc, is a glycosylphosphatidylinositol (GPI)-anchored membrane protein that is highly conserved in mammalian species. PrPc is expressed most abundantly in the brain, but has also been detected in other non-neuronal tissues such as muscle, lymphoid tissues and skin. Although PrPc was negatively or weakly expressed in the neck region of the gastric mucosa, it was found to be upregulated in the gastric mucosa of patients with Helicobacter pylori infection. Our previous data have demonstrated that PrPc was overexpressed in gastric cancer tissues, indicating a possible role of PrPc in occurrence and development of gastric cancer.Over the past years, many investigations have focused on PrPc functions in physiological and pathological processes. However, despite the abundant information about the function of misfold prion protein PrPsc, relatively poor characteristics is known about the function of PrPc. PrPc is targeted to lipid-riched microdomain, the so-called lipid raft, of the plasma membrane, the regions that are abundant in receptors and signaling molecules, consistent with a role of PrPc in cell adhesion and membrane signaling. It has been shown that PrPc bound some extracellular matrix and adhesive proteins, such as some glycosaminoglycans, laminin, N-CAM, laminin receptor and laminin receptor precursor. Moreover, PrPc... |